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Database: UniProt
Entry: CG121_METJA
LinkDB: CG121_METJA
Original site: CG121_METJA 
ID   CG121_METJA             Reviewed;         145 AA.
AC   Q57646;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=Regulatory protein Cgi121;
DE   AltName: Full=Positive regulator of Bud32 kinase activity;
GN   Name=cgi121; OrderedLocusNames=MJ0187;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN COMPLEX WITH KAE1-BUD32,
RP   STRUCTURE BY NMR, FUNCTION, SUBUNIT, AND MUTAGENESIS OF LEU-134; ALA-138
RP   AND LEU-139.
RX   PubMed=18951093; DOI=10.1016/j.molcel.2008.10.002;
RA   Mao D.Y., Neculai D., Downey M., Orlicky S., Haffani Y.Z., Ceccarelli D.F.,
RA   Ho J.S., Szilard R.K., Zhang W., Ho C.S., Wan L., Fares C., Rumpel S.,
RA   Kurinov I., Arrowsmith C.H., Durocher D., Sicheri F.;
RT   "Atomic structure of the KEOPS complex: an ancient protein kinase-
RT   containing molecular machine.";
RL   Mol. Cell 32:259-275(2008).
CC   -!- FUNCTION: Component of the KEOPS complex that is probably involved in
CC       the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP
CC       (TC-AMP) to the N6 group of A37, a step in the formation of a
CC       threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs
CC       that read codons beginning with adenine. Cgi121 stimulates Bud32 kinase
CC       activity via an activation of Bud32 autophosphorylation.
CC       {ECO:0000269|PubMed:18951093}.
CC   -!- SUBUNIT: Component of the KEOPS complex that consists of Kae1, Bud32,
CC       Cgi121 and Pcc1; the whole complex dimerizes.
CC       {ECO:0000269|PubMed:18951093}.
CC   -!- SIMILARITY: Belongs to the CGI121/TPRKB family. {ECO:0000305}.
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DR   EMBL; L77117; AAB98167.1; -; Genomic_DNA.
DR   PIR; D64323; D64323.
DR   RefSeq; WP_010869682.1; NC_000909.1.
DR   PDB; 2K8Y; NMR; -; A=1-145.
DR   PDB; 3ENH; X-ray; 3.60 A; C/D=1-145.
DR   PDB; 7KJT; X-ray; 3.34 A; H=1-145.
DR   PDBsum; 2K8Y; -.
DR   PDBsum; 3ENH; -.
DR   PDBsum; 7KJT; -.
DR   AlphaFoldDB; Q57646; -.
DR   BMRB; Q57646; -.
DR   SMR; Q57646; -.
DR   STRING; 243232.MJ_0187; -.
DR   PaxDb; 243232-MJ_0187; -.
DR   EnsemblBacteria; AAB98167; AAB98167; MJ_0187.
DR   GeneID; 1451034; -.
DR   KEGG; mja:MJ_0187; -.
DR   eggNOG; arCOG02197; Archaea.
DR   HOGENOM; CLU_1801715_0_0_2; -.
DR   InParanoid; Q57646; -.
DR   OrthoDB; 69587at2157; -.
DR   PhylomeDB; Q57646; -.
DR   EvolutionaryTrace; Q57646; -.
DR   Proteomes; UP000000805; Chromosome.
DR   Gene3D; 3.30.2380.10; CGI121/TPRKB; 1.
DR   InterPro; IPR013926; CGI121/TPRKB.
DR   InterPro; IPR036504; CGI121/TPRKB_sf.
DR   Pfam; PF08617; CGI-121; 1.
DR   SUPFAM; SSF143870; PF0523-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome.
FT   CHAIN           1..145
FT                   /note="Regulatory protein Cgi121"
FT                   /id="PRO_0000106735"
FT   MUTAGEN         134
FT                   /note="L->E: No effect on Bud32 binding."
FT                   /evidence="ECO:0000269|PubMed:18951093"
FT   MUTAGEN         134
FT                   /note="L->E: Severely affects Bud32 binding and does not
FT                   stimulate Bud32 kinase activity; when associated with R-
FT                   138."
FT                   /evidence="ECO:0000269|PubMed:18951093"
FT   MUTAGEN         138
FT                   /note="A->R: No effect on Bud32 binding."
FT                   /evidence="ECO:0000269|PubMed:18951093"
FT   MUTAGEN         138
FT                   /note="A->R: Severely affects Bud32 binding and does not
FT                   stimulate Bud32 kinase activity; when associated with E-
FT                   134."
FT                   /evidence="ECO:0000269|PubMed:18951093"
FT   MUTAGEN         139
FT                   /note="L->R: No effect on Bud32 binding."
FT                   /evidence="ECO:0000269|PubMed:18951093"
FT   STRAND          2..9
FT                   /evidence="ECO:0007829|PDB:7KJT"
FT   HELIX           13..17
FT                   /evidence="ECO:0007829|PDB:7KJT"
FT   STRAND          21..26
FT                   /evidence="ECO:0007829|PDB:7KJT"
FT   HELIX           27..29
FT                   /evidence="ECO:0007829|PDB:7KJT"
FT   HELIX           33..45
FT                   /evidence="ECO:0007829|PDB:7KJT"
FT   STRAND          49..52
FT                   /evidence="ECO:0007829|PDB:7KJT"
FT   HELIX           53..62
FT                   /evidence="ECO:0007829|PDB:7KJT"
FT   HELIX           67..74
FT                   /evidence="ECO:0007829|PDB:7KJT"
FT   STRAND          78..87
FT                   /evidence="ECO:0007829|PDB:7KJT"
FT   HELIX           88..98
FT                   /evidence="ECO:0007829|PDB:7KJT"
FT   HELIX           104..107
FT                   /evidence="ECO:0007829|PDB:7KJT"
FT   HELIX           111..120
FT                   /evidence="ECO:0007829|PDB:7KJT"
FT   STRAND          125..127
FT                   /evidence="ECO:0007829|PDB:7KJT"
FT   HELIX           129..138
FT                   /evidence="ECO:0007829|PDB:7KJT"
FT   HELIX           139..141
FT                   /evidence="ECO:0007829|PDB:7KJT"
SQ   SEQUENCE   145 AA;  16593 MW;  E7CB7330D1E1003F CRC64;
     MIIRGIRGAR INNEIFNLGL KFQILNADVV ATKKHVLHAI NQAKTKKPIA KSFWMEILVR
     ASGQRQIHEA IKIIGAKDGN VCLICEDEET FRKIYELIGG EIDDSVLEIN EDKERLIREI
     FKIRGFGNVV ERVLEKIALI ELKKE
//
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